Thioredoxin 1 Is Inactivated Due to Oxidation Induced by Peroxiredoxin under Oxidative Stress and Reactivated by the Glutaredoxin System

Du, Yu‐Cang; Zhang, Huihui; Zhang, Xu; Lu, Jun; Holmgren, Arne

doi:10.1074/jbc.m113.495150

Cited by 90 publications

(99 citation statements)

References 51 publications

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“…In the intracellular compartment, TRX-1 was mainly present as nonfully oxidized forms in basal conditions. In this respect, there have been previous papers showing only the reduced form of TRX-1 in basal conditions [24,[42][43][44][45], while others also ͳͳ showed the two bands observed in the present paper [46,47]. Technical questions and/or culture conditions could account for these potential discrepancies since it has been demonstrated that proliferative status [48] or ion composition [49] could modify TRX-1 oxidative status.…”

Section: Discussionsupporting

confidence: 45%

Thioredoxin-1/peroxiredoxin-1 as sensors of oxidative stress mediated by NADPH oxidase activity in atherosclerosis

Madrigal‐Matute

Fernandez-Garcia

Blanco-Colio

et al. 2015

Free Radical Biology and Medicine

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Section: Discussionsupporting

confidence: 45%

Thioredoxin-1/peroxiredoxin-1 as sensors of oxidative stress mediated by NADPH oxidase activity in atherosclerosis

Madrigal‐Matute

Fernandez-Garcia

Blanco-Colio

et al. 2015

Free Radical Biology and Medicine

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“…The redox state of Trx was detected using a modified Western blot analysis [37]. Briefly, Jurkat For the determination of Prx3 redox state, after incubation with 1 (50µM) and 2 (15 µM) for 18 h, Jurkat cells were collected, centrifuged at 500 g for 5 min, washed with cold PBS and then treated with 1 mL of 10% trichloro-acetic acid.…”

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confidence: 99%

Osmocenyl-tamoxifen derivatives target the thioredoxin system leading to a redox imbalance in Jurkat cells

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Lee

et al. 2016

Journal of Inorganic Biochemistry

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ABSTRACT:To complete our study of the iron, ruthenium and osmium metallocene triad derived from hydroxytamoxifen, we report here the synthesis and study of the biological effects of two ferrocifen analogs in the osmium series, namely the monophenolic complex 1, the tamoxifen- within the cell and that inhibition of thioredoxin reductase is a key factor in rationalizing the cytotoxicity of these complexes on Jurkat cells.

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“…The neglect of alternative H 2 O 2 sinks is a conservative assumption with respect to the H 2 O 2 attained in the cytoplasm. Third, it neglects thioredoxin oxidation, as the redox capacity of most cells is sufficient to keep thioredoxin reduced in absence of strong oxidative stress [16,44,40,18]. Fourth, it accounts for a single 2-Cys peroxiredoxin whose concentration represents the sum of PrxI and PrxII, the two 2-Cys peroxiredoxins that are abundant in the cytoplasm of most mammalian cells [11].…”

Section: Models and Methodsmentioning

confidence: 99%

Localized redox relays as a privileged mode of cytoplasmic hydrogen peroxide signaling

Travasso

Aidos

Abranches

et al. 2017

Free Radical Biology and Medicine

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A B S T R A C THydrogen peroxide (H 2 O 2 ) is a key signaling agent. Its best characterized signaling actions in mammalian cells involve the early oxidation of thiols in cytoplasmic phosphatases, kinases and transcription factors. However, these redox targets are orders of magnitude less H 2 O 2 -reactive and abundant than cytoplasmic peroxiredoxins. How can they be oxidized in a signaling time frame? Here we investigate this question using computational reaction-diffusion models of H 2 O 2 signaling. The results show that at H 2 O 2 supply rates commensurate with mitogenic signaling a H 2 O 2 concentration gradient with a length scale of a few tenths of μm is established. Even near the supply sites H 2 O 2 concentrations are far too low to oxidize typical targets in an early mitogenic signaling time frame. Furthermore, any inhibition of the peroxiredoxin or increase in H 2 O 2 supply able to drastically increase the local H 2 O 2 concentration would collapse the concentration gradient and/or cause an extensive oxidation of the peroxiredoxins I and II, inconsistent with experimental observations. In turn, the local concentrations of peroxiredoxin sulfenate and disulfide forms exceed those of H 2 O 2 by several orders of magnitude. Redox targets reacting with these forms at rate constants much lower than that for, say, thioredoxin could be oxidized within seconds. Moreover, the spatial distribution of the concentrations of these peroxiredoxin forms allows them to reach targets within 1 μm from the H 2 O 2 sites while maintaining signaling localized. The recruitment of peroxiredoxins to specific sites such as caveolae can dramatically increase the local concentrations of the sulfenic and disulfide forms, thus further helping these species to outcompete H 2 O 2 for the oxidation of redox targets. Altogether, these results suggest that H 2 O 2 signaling is mediated by localized redox relays whereby peroxiredoxins are oxidized to sulfenate and disulfide forms at H 2 O 2 supply sites and these forms in turn oxidize the redox targets near these sites.

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Thioredoxin 1 Is Inactivated Due to Oxidation Induced by Peroxiredoxin under Oxidative Stress and Reactivated by the Glutaredoxin System

Cited by 90 publications

References 51 publications

Thioredoxin-1/peroxiredoxin-1 as sensors of oxidative stress mediated by NADPH oxidase activity in atherosclerosis

Thioredoxin-1/peroxiredoxin-1 as sensors of oxidative stress mediated by NADPH oxidase activity in atherosclerosis

Osmocenyl-tamoxifen derivatives target the thioredoxin system leading to a redox imbalance in Jurkat cells

Localized redox relays as a privileged mode of cytoplasmic hydrogen peroxide signaling

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